D
David M. Ogrydziak
Researcher at University of California, Davis
Publications - 29
Citations - 972
David M. Ogrydziak is an academic researcher from University of California, Davis. The author has contributed to research in topics: Yarrowia & Gene. The author has an hindex of 18, co-authored 29 publications receiving 946 citations.
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Journal ArticleDOI
Yeast Extracellular Proteases
TL;DR: Results obtained from the sequences of cloned genes, especially the Saccharomyces cerevisiae Bar protease, the Candida albicans acid proteases, and the Yarrowia lipolytica alkaline protease have been emphasized.
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Alkaline extracellular protease produced by Saccharomycopsis lipolytica CX161-1B.
TL;DR: The alkaline protease was purified to homogeneity (as determined by polyacrylamide gel electrophoresis) by ultrafiltration, gel filtration and DEAE-cellulose chromatography, and not inhibited by dithiothreitol, N-ethylmaleimide or 4-hydroxymercuribenzoic acid, indicating that it is a serine protease.
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Construction of Lactose-Assimilating and High-Ethanol-Producing Yeasts by Protoplast Fusion
TL;DR: The protoplast fusion technique is used to construct hybrids between auxotrophic strains of S. cerevisiae having high ethanol tolerance and an auxotrophe strain of lactose-fermenting K. fragilis isolated by ethyl methanesulfonate mutagenesis, which were prototrophic and capable of assimilating lactose and producing ethanol in excess of 13% (vol/vol).
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Expression, Secretion, and Processing of Rice α-Amylase in the Yeast Yarrowia lipolytica
TL;DR: Results suggest that the XPR2 pro-region is dispensable for obtaining the precise N-terminal amino acid in heterologous protein secretion.
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Cloning, nucleotide sequence and functions of XPR6, which codes for a dibasic processing endoprotease from the yeast Yarrowia lipolytica.
TL;DR: The XPR6 gene was cloned by complementation by screening for restoration of production of alkaline protease activity and revealed a large open reading frame with a coding capacity of 976 amino acids that had significant homology to Saccharomyces cerevisiae Kex2p, a processing endoprotease that cleaves after pairs of basic amino acids.